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在大肠杆菌正常蛋白质分泌过程中,SecA蛋白会自身抑制其自身的翻译。

SecA protein autogenously represses its own translation during normal protein secretion in Escherichia coli.

作者信息

Schmidt M G, Oliver D B

机构信息

Department of Microbiology, State University of New York, Stony Brook 11794.

出版信息

J Bacteriol. 1989 Feb;171(2):643-9. doi: 10.1128/jb.171.2.643-649.1989.

Abstract

The Escherichia coli secA gene, whose expression is responsive to the protein secretion status of the cell, is the second gene in an operon. We found that both the basal and induced levels of SecA biosynthesis are dependent on prior translation of the upstream gene, gene X, and identified two large gene X-secA transcripts. The 10-fold derepression of secA expression by protein export defects was at the translational level since no further increases in gene X or secA mRNA levels were detected during this period, and a secA-lacZ protein fusion but not an operon fusion was appropriately derepressed. Furthermore, overexpression of the SecA protein severely reduced expression of only the secA-lacZ protein fusion, indicating that SecA autogenously represses its own translation.

摘要

大肠杆菌的secA基因是一个操纵子中的第二个基因,其表达对细胞的蛋白质分泌状态有反应。我们发现,SecA生物合成的基础水平和诱导水平均依赖于上游基因X的先翻译,并鉴定出两种大的基因X-secA转录本。由于在此期间未检测到基因X或secA mRNA水平的进一步增加,且secA-lacZ蛋白融合体而非操纵子融合体被适当去阻遏,因此蛋白质输出缺陷导致的secA表达10倍去阻遏发生在翻译水平。此外,SecA蛋白的过表达仅严重降低了secA-lacZ蛋白融合体的表达,表明SecA自身抑制其自身的翻译。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/668e/209645/4a84bbf07cb1/jbacter00168-0035-a.jpg

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